Is there a dynamic protein contribution to the substrate trigger in coenzyme B 12-dependent ethanolamine ammonia lyase?

    Research output: Contribution to journalArticlepeer-review

    Abstract

    "Cohort-ry" in motion: The chemistry following Co-C bond homolysis in coenzyme B 12-dependent ethanolamine ammonia lyase is known to favor dissociation, but what of the protein contribution? Experiments reveal the radical pair reaction dynamics to be coupled to the ps-ns protein dynamics in B 12 photolysis. This raises the possibility of a subtle, dynamic contribution to homolysis, which acts in cohort with electrostatics and H-abstraction from the substrate. © 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
    Original languageEnglish
    Pages (from-to)10843-10846
    Number of pages3
    JournalAngewandte Chemie - International Edition
    Volume50
    Issue number46
    DOIs
    Publication statusPublished - 11 Nov 2011

    Keywords

    • coenzyme B 12
    • enzyme catalysis
    • magnetic field effects
    • protein dynamics
    • radical pair reactions

    Research Beacons, Institutes and Platforms

    • Photon Science Institute

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